WTAP and m
Humans
RNA, Circular
/ genetics
Leukemia, Myeloid, Acute
/ genetics
Adenosine
/ analogs & derivatives
Oxidative Stress
/ drug effects
Bortezomib
/ pharmacology
Cell Line, Tumor
Reactive Oxygen Species
/ metabolism
RNA Splicing Factors
/ metabolism
Cell Cycle Proteins
/ metabolism
Neoplastic Stem Cells
/ metabolism
Heme Oxygenase-1
/ metabolism
Protein Serine-Threonine Kinases
Intracellular Signaling Peptides and Proteins
AML
Oxidative stress
WTAP
circHIPK3
circRNAs
m6A
Journal
Cellular and molecular life sciences : CMLS
ISSN: 1420-9071
Titre abrégé: Cell Mol Life Sci
Pays: Switzerland
ID NLM: 9705402
Informations de publication
Date de publication:
23 Jun 2024
23 Jun 2024
Historique:
received:
23
03
2024
accepted:
27
05
2024
revised:
19
05
2024
medline:
23
6
2024
pubmed:
23
6
2024
entrez:
23
6
2024
Statut:
epublish
Résumé
N
Identifiants
pubmed: 38909325
doi: 10.1007/s00018-024-05299-9
pii: 10.1007/s00018-024-05299-9
doi:
Substances chimiques
RNA, Circular
0
Adenosine
K72T3FS567
N-methyladenosine
CLE6G00625
WTAP protein, human
0
Bortezomib
69G8BD63PP
Reactive Oxygen Species
0
RNA Splicing Factors
0
HIPK3 protein, human
EC 2.7.11.1
Cell Cycle Proteins
0
Heme Oxygenase-1
EC 1.14.14.18
Protein Serine-Threonine Kinases
EC 2.7.11.1
Intracellular Signaling Peptides and Proteins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
276Subventions
Organisme : Fondazione AIRC per la ricerca sul cancro ETS
ID : IG 2018-ID21434
Organisme : Fondazione AIRC per la ricerca sul cancro ETS
ID : 2019-ID: 22759
Organisme : Fondazione AIRC per la ricerca sul cancro ETS
ID : IG 2018-ID 21406
Organisme : PRIN
ID : 2022-Prot. 2022WB59LB
Organisme : Sapienza Università di Roma
ID : "Progetti Ateneo"
Organisme : PNRR
ID : NextGenerationEU DD. 3175/2021 E DD. 3138/2021 CN_3: National Center for Gene Therapy
Organisme : PNRR
ID : Drugs based on RNA Technology Codice Progetto CN 00000041
Informations de copyright
© 2024. The Author(s).
Références
Desrosiers R, Friderici K, Rottman F (1974) Identification of methylated nucleosides in messenger RNA from Novikoff hepatoma cells. Proc Natl Acad Sci USA 71:3971. https://doi.org/10.1073/PNAS.71.10.3971
doi: 10.1073/PNAS.71.10.3971
pubmed: 4372599
pmcid: 434308
Bokar JA, Shambaugh ME, Polayes D et al (1997) Purification and cDNA cloning of the AdoMet-binding subunit of the human mRNA (N6-adenosine)-methyltransferase. RNA 3:1233–1247
pubmed: 9409616
pmcid: 1369564
Wang S, Lv W, Li T et al (2022) Dynamic regulation and functions of mRNA m6A modification. Cancer Cell Int 22, 48. https://doi.org/10.1186/s12935-022-02452-x
doi: 10.1186/s12935-022-02452-x
pubmed: 35093087
pmcid: 8800407
Dominissini D, Moshitch-Moshkovitz S, Schwartz S et al (2012) Topology of the human and mouse m6A RNA methylomes revealed by m6A-seq. Nature 485:201–206. https://doi.org/10.1038/nature11112
doi: 10.1038/nature11112
pubmed: 22575960
Csepanys T, Lint A, Baldick CJ, Beemonq K (1990) Sequence specificity of mRNA N6-adenosine methyltransferase. J Biol Chem 265:20117–20122. https://doi.org/10.1016/S0021-9258(17)30477-5
doi: 10.1016/S0021-9258(17)30477-5
Śledź P, Jinek M (2016) Structural insights into the molecular mechanism of the m6A writer complex. Elife 5:e18434. https://doi.org/10.7554/eLife.18434
doi: 10.7554/eLife.18434
pubmed: 27627798
pmcid: 5023411
Lesbirel S, Wilson SA (2019) The m6A-methylase complex and mRNA export. Biochim Biophys Acta Gene Regul Mech 1862:319. https://doi.org/10.1016/J.BBAGRM.2018.09.008
doi: 10.1016/J.BBAGRM.2018.09.008
pubmed: 30290229
pmcid: 6414750
Jia G, Fu Y, Zhao X et al (2011) N6-Methyladenosine in nuclear RNA is a major substrate of the obesity-associated FTO. Nat Chem Biol 7:885–887. https://doi.org/10.1038/nchembio.687
doi: 10.1038/nchembio.687
pubmed: 22002720
pmcid: 3218240
Zheng G, Dahl JA, Niu Y et al (2013) ALKBH5 is a mammalian RNA demethylase that impacts RNA metabolism and mouse fertility. Mol Cell 49:18–29. https://doi.org/10.1016/j.molcel.2012.10.015
doi: 10.1016/j.molcel.2012.10.015
pubmed: 23177736
Liao S, Sun H, Xu C (2018) YTH domain: a family of N6-methyladenosine (m6A) readers. Genom Proteom Bioinform 16:99–107. https://doi.org/10.1016/J.GPB.2018.04.002
doi: 10.1016/J.GPB.2018.04.002
Rajagopalan LE, Westmark CJ, Jarzembowski JA, Malter JS (1998) hnRNP C increases amyloid precursor protein (APP) production by stabilizing APP mRNA. Nucl Acids Res 26:3418–3423. https://doi.org/10.1093/NAR/26.14.3418
doi: 10.1093/NAR/26.14.3418
pubmed: 9649628
pmcid: 147701
Zarnack K, König J, Tajnik M et al (2013) Direct competition between hnRNP C and U2AF65 protects the transcriptome from the exonization of Alu elements. Cell 152:453–466. https://doi.org/10.1016/J.CELL.2012.12.023
doi: 10.1016/J.CELL.2012.12.023
pubmed: 23374342
pmcid: 3629564
McCloskey A, Taniguchi I, Shinmyozu K, Ohno M (2012) hnRNP C tetramer measures RNA length to classify RNA polymerase II transcripts for export. Science 335:1643–1646. https://doi.org/10.1126/SCIENCE.1218469
doi: 10.1126/SCIENCE.1218469
pubmed: 22461616
Huang H, Weng H, Sun W et al (2018) Recognition of RNA N6-methyladenosine by IGF2BP proteins enhances mRNA stability and translation. Nat Cell Biol 20:285. https://doi.org/10.1038/S41556-018-0045-Z
doi: 10.1038/S41556-018-0045-Z
pubmed: 29476152
pmcid: 5826585
Fazi F, Fatica A (2019) Interplay between N6-methyladenosine (m6A) and non-coding RNAs in cell development and cancer. Front Cell Dev Biol 7:116. https://doi.org/10.3389/fcell.2019.00116
doi: 10.3389/fcell.2019.00116
pubmed: 31316981
pmcid: 6611489
Fustin JM, Doi M, Yamaguchi Y et al (2013) XRNA-methylation-dependent RNA processing controls the speed of the circadian clock. Cell 155:793. https://doi.org/10.1016/j.cell.2013.10.026
doi: 10.1016/j.cell.2013.10.026
pubmed: 24209618
Jiang X, Liu B, Nie Z et al (2021) The role of m6A modification in the biological functions and diseases. Signal Transduct Target Ther 61(6):1–16. https://doi.org/10.1038/s41392-020-00450-x
doi: 10.1038/s41392-020-00450-x
Showel MM, Levis M (2014) Advances in treating acute myeloid leukemia. F1000Prime Rep. https://doi.org/10.12703/P6-96
doi: 10.12703/P6-96
pubmed: 25374674
pmcid: 4191225
Thein MS, Ershler WB, Jemal A et al (2013) Outcome of older patients with acute myeloid leukemia: an analysis of SEER data over 3 decades. Cancer 119:2720–2727. https://doi.org/10.1002/CNCR.28129
doi: 10.1002/CNCR.28129
pubmed: 23633441
Dores GM, Devesa SS, Curtis RE et al (2012) Acute leukemia incidence and patient survival among children and adults in the United States, 2001–2007. Blood 119:34–43. https://doi.org/10.1182/BLOOD-2011-04-347872
doi: 10.1182/BLOOD-2011-04-347872
pubmed: 22086414
pmcid: 3251235
Levis M, Murphy KM, Pham R et al (2005) Internal tandem duplications of the FLT3 gene are present in leukemia stem cells. Blood 106:673. https://doi.org/10.1182/BLOOD-2004-05-1902
doi: 10.1182/BLOOD-2004-05-1902
pubmed: 15797998
pmcid: 1895185
Takahashi S (2020) Mutations of FLT3 receptor affect its surface glycosylation, intracellular localization, and downstream signaling. Leuk Res Reports 13:100187. https://doi.org/10.1016/J.LRR.2019.100187
doi: 10.1016/J.LRR.2019.100187
Liquori A, Ibañez M, Sargas C et al (2020) Acute promyelocytic leukemia: a constellation of molecular events around a single PML-RARA fusion gene. Cancers (Basel). https://doi.org/10.3390/CANCERS12030624
doi: 10.3390/CANCERS12030624
pubmed: 32182684
Meyer C, Schneider B, Jakob S et al (2006) The MLL recombinome of acute leukemias. Leukemia 20:777–784. https://doi.org/10.1038/SJ.LEU.2404150
doi: 10.1038/SJ.LEU.2404150
pubmed: 16511515
Gardner BM, Pincus D, Gotthardt K et al (2013) Endoplasmic reticulum stress sensing in the unfolded protein response. Cold Spring Harb Perspect Biol. https://doi.org/10.1101/CSHPERSPECT.A013169
doi: 10.1101/CSHPERSPECT.A013169
pubmed: 23388626
pmcid: 3578356
Martelli A, Paganelli F, Chiarini F et al (2020) The unfolded protein response: a novel therapeutic target in acute leukemias. Cancers (Basel) 12:333. https://doi.org/10.3390/cancers12020333
doi: 10.3390/cancers12020333
pubmed: 32024211
Tsai YC, Weissman AM (2010) The unfolded protein response, degradation from the endoplasmic reticulum, and cancer. Genes Cancer. https://doi.org/10.1177/1947601910383011
doi: 10.1177/1947601910383011
pubmed: 21331300
pmcid: 3039444
Spano J-P, Bay J-O, Blay J-Y, Rixe O (2005) Proteasome inhibition: a new approach for the treatment of malignancies. Bull Cancer 92(E61–6):945–952
Alwahsh M, Farhat J, Talhouni S et al (2023) Bortezomib advanced mechanisms of action in multiple myeloma, solid and liquid tumors along with its novel therapeutic applications. Excli J 22:146–168. https://doi.org/10.17179/excli2022-5653
doi: 10.17179/excli2022-5653
pubmed: 36998701
pmcid: 10043448
Liccardo F, Śniegocka M, Tito C et al (2023) Retinoic acid and proteotoxic stress induce AML cell death overcoming stromal cell protection. J Exp Clin Cancer Res. https://doi.org/10.1186/S13046-023-02793-Z
doi: 10.1186/S13046-023-02793-Z
pubmed: 37653435
pmcid: 10469880
Śniegocka M, Liccardo F, Fazi F, Masciarelli S (2022) Understanding ER homeostasis and the UPR to enhance treatment efficacy of acute myeloid leukemia. Drug Resist Upd. https://doi.org/10.1016/J.DRUP.2022.100853
doi: 10.1016/J.DRUP.2022.100853
Lopez-Reyes RG, Quinet G, Gonzalez-Santamarta M et al (2021) Inhibition of the proteasome and proteaphagy enhances apoptosis in FLT3-ITD-driven acute myeloid leukemia. FEBS Open Bio 11:48–60. https://doi.org/10.1002/2211-5463.12950
doi: 10.1002/2211-5463.12950
pubmed: 33410599
Li X, Yang L, Chen LL (2018) The biogenesis, functions, and challenges of circular RNAs. Mol Cell 71:428–442. https://doi.org/10.1016/J.MOLCEL.2018.06.034
doi: 10.1016/J.MOLCEL.2018.06.034
pubmed: 30057200
Jamal M, Song T, Chen B et al (2019) Recent progress on circular RNA research in acute myeloid leukemia. Front Oncol. https://doi.org/10.3389/FONC.2019.01108
doi: 10.3389/FONC.2019.01108
pubmed: 31781482
pmcid: 6851197
Liccardo F, Iaiza A, Śniegocka M et al (2022) Circular RNAs activity in the leukemic bone marrow microenvironment. Non-coding RNA 8:50. https://doi.org/10.3390/NCRNA8040050
doi: 10.3390/NCRNA8040050
pubmed: 35893233
pmcid: 9326527
Wu J, Guo X, Wen Y et al (2021) N6-methyladenosine modification opens a new chapter in circular RNA biology. Front Cell Dev Biol. https://doi.org/10.3389/FCELL.2021.709299
doi: 10.3389/FCELL.2021.709299
pubmed: 35252214
pmcid: 8740065
Di Timoteo G, Dattilo D, Centrón-Broco A et al (2020) Modulation of circRNA metabolism by m6A modification. Cell Rep. https://doi.org/10.1016/j.celrep.2020.107641
doi: 10.1016/j.celrep.2020.107641
pubmed: 32402287
Wei J, Harada BT, Lu D et al (2021) HRD1-mediated METTL14 degradation regulates m6A mRNA modification to suppress ER proteotoxic liver disease. Mol Cell 81:5052-5065.e6. https://doi.org/10.1016/J.MOLCEL.2021.10.028
doi: 10.1016/J.MOLCEL.2021.10.028
pubmed: 34847358
pmcid: 8751812
Li Q, Li X, Tang H et al (2017) NSUN2-mediated m5C methylation and METTL3/METTL14-mediated m6A methylation cooperatively enhance p21 translation. J Cell Biochem 118:2587. https://doi.org/10.1002/JCB.25957
doi: 10.1002/JCB.25957
pubmed: 28247949
pmcid: 5509477
Zhao T, Li X, Sun D, Zhang Z (2019) Oxidative stress: One potential factor for arsenite-induced increase of N6-methyladenosine in human keratinocytes. Environ Toxicol Pharmacol 69:95–103. https://doi.org/10.1016/J.ETAP.2019.04.005
doi: 10.1016/J.ETAP.2019.04.005
pubmed: 31004932
Sun L, Wan A, Zhou Z et al (2021) RNA-binding protein RALY reprogrammes mitochondrial metabolism via mediating miRNA processing in colorectal cancer. Gut 70:1698–1712. https://doi.org/10.1136/GUTJNL-2020-320652
doi: 10.1136/GUTJNL-2020-320652
pubmed: 33219048
Wang J, Ishfaq M, Xu L et al (2019) METTL3/m6A/miRNA-873-5p attenuated oxidative stress and apoptosis in colistin-induced kidney injury by modulating Keap1/Nrf2 pathway. Front Pharmacol. https://doi.org/10.3389/FPHAR.2019.00517/FULL
doi: 10.3389/FPHAR.2019.00517/FULL
pubmed: 32153390
pmcid: 6933012
Ewels P, Magnusson M, Lundin S, Käller M (2016) MultiQC: summarize analysis results for multiple tools and samples in a single report. Bioinformatics 32:3047–3048. https://doi.org/10.1093/BIOINFORMATICS/BTW354
doi: 10.1093/BIOINFORMATICS/BTW354
pubmed: 27312411
pmcid: 5039924
Dobin A, Davis CA, Schlesinger F et al (2013) STAR: ultrafast universal RNA-seq aligner. Bioinformatics 29:15–21. https://doi.org/10.1093/BIOINFORMATICS/BTS635
doi: 10.1093/BIOINFORMATICS/BTS635
pubmed: 23104886
Li H, Handsaker B, Wysoker A et al (2009) The sequence alignment/map format and SAMtools. Bioinforma Appl Note 25:2078–2079. https://doi.org/10.1093/bioinformatics/btp352
doi: 10.1093/bioinformatics/btp352
Ma XK, Xue W, Chen LL, Yang L (2021) CIRCexplorer pipelines for circRNA annotation and quantification from non-polyadenylated RNA-seq datasets. Methods 196:3–10. https://doi.org/10.1016/J.YMETH.2021.02.008
doi: 10.1016/J.YMETH.2021.02.008
pubmed: 33588028
Zhang J, Chen S, Yang J (2020) Zhao F (2020) Accurate quantification of circular RNAs identifies extensive circular isoform switching events. Nat Commun 111(11):1–14. https://doi.org/10.1038/s41467-019-13840-9
doi: 10.1038/s41467-019-13840-9
Robinson MD, Mccarthy DJ, Smyth GK (2010) edgeR: a Bioconductor package for differential expression analysis of digital gene expression data. Bioinforma Appl NOTE 26:139–140. https://doi.org/10.1093/bioinformatics/btp616
doi: 10.1093/bioinformatics/btp616
Chen M, Xie S (2018) Therapeutic targeting of cellular stress responses in cancer. Thorac Cancer 9:1575. https://doi.org/10.1111/1759-7714.12890
doi: 10.1111/1759-7714.12890
pubmed: 30312004
pmcid: 6275842
Cheng Y, Xie W, Pickering BF et al (2021) N 6-Methyladenosine on mRNA facilitates a phase-separated nuclear body that suppresses myeloid leukemic differentiation. Cancer Cell 39:958–972. https://doi.org/10.1016/j.ccell.2021.04.017
doi: 10.1016/j.ccell.2021.04.017
pubmed: 34048709
pmcid: 8282764
Wang J, Qiao Y, Sun M et al (2022) FTO promotes colorectal cancer progression and chemotherapy resistance via demethylating G6PD/PARP1. Clin Transl Med 12:e772. https://doi.org/10.1002/CTM2.772
doi: 10.1002/CTM2.772
pubmed: 35297218
pmcid: 8926902
Lin Z, Wan AH, Sun L et al (2023) N6-methyladenosine demethylase FTO enhances chemo-resistance in colorectal cancer through SIVA1-mediated apoptosis. Mol Ther. https://doi.org/10.1016/j.ymthe.2022.10.012
doi: 10.1016/j.ymthe.2022.10.012
pubmed: 38140726
pmcid: 10278048
Way SW, Popko B (2016) Harnessing the integrated stress response for the treatment of multiple sclerosis. Lancet Neurol 15:434–443. https://doi.org/10.1016/S1474-4422(15)00381-6
doi: 10.1016/S1474-4422(15)00381-6
pubmed: 26873788
pmcid: 4792730
Schmidt EK, Clavarino G, Ceppi M, Pierre P (2009) SUnSET, a nonradioactive method to monitor protein synthesis. Nat Methods 6:275–277. https://doi.org/10.1038/NMETH.1314
doi: 10.1038/NMETH.1314
pubmed: 19305406
Zhang Y, Chen Y, Wan Y et al (2021) Circular RNAs in the regulation of oxidative stress. Front Pharmacol. https://doi.org/10.3389/FPHAR.2021.697903
doi: 10.3389/FPHAR.2021.697903
pubmed: 35757387
pmcid: 8758560
Park SM, Il KT, So JS (2021) Roles of XBP1s in transcriptional regulation of target genes. Biomedicines. https://doi.org/10.3390/BIOMEDICINES9070791
doi: 10.3390/BIOMEDICINES9070791
pubmed: 35052706
pmcid: 8773309
Loke J, Buka R, Craddock C (2021) Allogeneic stem cell transplantation for acute myeloid leukemia: who, when, and how? Front Immunol 12:1182. https://doi.org/10.3389/FIMMU.2021.659595/BIBTEX
doi: 10.3389/FIMMU.2021.659595/BIBTEX
Féral K, Jaud M, Philippe C et al (2021) ER stress and unfolded protein response in leukemia: friend, foe, or both? Biomolecules 11:1–31. https://doi.org/10.3390/BIOM11020199
doi: 10.3390/BIOM11020199
Hetz C, Chevet E (2015) Theme series—UPR in cancer. Semin Cancer Biol 33:1–2. https://doi.org/10.1016/J.SEMCANCER.2015.04.008
doi: 10.1016/J.SEMCANCER.2015.04.008
pubmed: 25957480
Doultsinos D, Avril T, Lhomond S et al (2017) Control of the unfolded protein response in health and disease. SLAS Discov Adv life Sci R D 22:787–800. https://doi.org/10.1177/2472555217701685
doi: 10.1177/2472555217701685
Masciarelli S, Capuano E, Ottone T et al (2018) Retinoic acid and arsenic trioxide sensitize acute promyelocytic leukemia cells to ER stress. Leukemia. https://doi.org/10.1038/leu.2017.231
doi: 10.1038/leu.2017.231
pubmed: 28776567
Greene J, Baird AM, Brady L et al (2017) Circular RNAs: biogenesis, function and role in human diseases. Front Mol Biosci 4:38. https://doi.org/10.3389/FMOLB.2017.00038
doi: 10.3389/FMOLB.2017.00038
pubmed: 28634583
pmcid: 5459888
Legnini I, Di Timoteo G, Rossi F et al (2017) Circ-ZNF609 is a circular RNA that can be translated and functions in myogenesis. Mol Cell 66:22-37.e9. https://doi.org/10.1016/J.MOLCEL.2017.02.017
doi: 10.1016/J.MOLCEL.2017.02.017
pubmed: 28344082
pmcid: 5387670
Yang Y, Fan X, Mao M et al (2017) Extensive translation of circular RNAs driven by N 6-methyladenosine. Cell Res 27:626–641. https://doi.org/10.1038/CR.2017.31
doi: 10.1038/CR.2017.31
pubmed: 28281539
pmcid: 5520850
Little NA, Hastie ND, Davies RC (2000) Identification of WTAP, a novel Wilms’ tumour 1-associating protein. Hum Mol Genet 9:2231–2239. https://doi.org/10.1093/OXFORDJOURNALS.HMG.A018914/2/DDD25707.JPEG
doi: 10.1093/OXFORDJOURNALS.HMG.A018914/2/DDD25707.JPEG
pubmed: 11001926
Naren D, Yan T, Gong Y et al (2021) High Wilms’ tumor 1 associating protein expression predicts poor prognosis in acute myeloid leukemia and regulates m 6 A methylation of MYC mRNA. J Cancer Res Clin Oncol 147:33–47. https://doi.org/10.1007/S00432-020-03373-W
doi: 10.1007/S00432-020-03373-W
pubmed: 32880751
Zhang L, Khadka B, Wu J et al (2021) Bone marrow mesenchymal stem cells-derived exosomal miR-425-5p inhibits acute myeloid leukemia cell proliferation, apoptosis, invasion and migration by targeting WTAP. Onco Targets Ther 14:4901–4914. https://doi.org/10.2147/OTT.S286326
doi: 10.2147/OTT.S286326
pubmed: 34594112
pmcid: 8478487
Yin F, Liu K, Peng W et al (2023) The effect of N6-methyladenosine regulators and m6A reader YTHDC1-mediated N6-methyladenosine modification is involved in oxidative stress in human aortic dissection. Oxid Med. https://doi.org/10.1155/2023/3918393
doi: 10.1155/2023/3918393
Wu J, Wang X, Li X (2023) N6-methyladenosine methylation regulator FTO promotes oxidative stress and induces cell apoptosis in ovarian cancer. Epigenomics 14:1509–1522. https://doi.org/10.2217/EPI-2022-0403
doi: 10.2217/EPI-2022-0403
Pedre B, Barayeu U, Ezeriņa D, Dick TP (2021) The mechanism of action of N-acetylcysteine (NAC): the emerging role of H2S and sulfane sulfur species. Pharmacol Ther 228:107916. https://doi.org/10.1016/J.PHARMTHERA.2021.107916
doi: 10.1016/J.PHARMTHERA.2021.107916
pubmed: 34171332
Yang B, Chen Q (2021) Cross-talk between oxidative stress and m 6 A RNA methylation in cancer. Oxid Med Cell Longev. https://doi.org/10.1155/2021/6545728
doi: 10.1155/2021/6545728
pubmed: 36226158
pmcid: 8741347
Wang Y, Zhao R, Liu W et al (2019) Exosomal circHIPK3 released from hypoxia-pretreated cardiomyocytes regulates oxidative damage in cardiac microvascular endothelial cells via the miR-29a/IGF-1 pathway. Oxid Med Cell Longev. https://doi.org/10.1155/2019/7954657
doi: 10.1155/2019/7954657
pubmed: 33273997
pmcid: 6955139
Ge R, Gao G (2020) Anti-antioxidant impacts of circZNF609 silence in HaCaT cells through regulating miR-145. Artif Cell Nanomed Biotechnol 48:384–392. https://doi.org/10.1080/21691401.2019.1709863
doi: 10.1080/21691401.2019.1709863
Liu X, Liu X, Cai M et al (2021) CircRNF220, not its linear cognate gene RNF220, regulates cell growth and is associated with relapse in pediatric acute myeloid leukemia. Mol Cancer 20:1–18. https://doi.org/10.1186/S12943-021-01395-7/FIGURES/6
doi: 10.1186/S12943-021-01395-7/FIGURES/6
Richard-Carpentier G, DiNardo CD (2019) Venetoclax for the treatment of newly diagnosed acute myeloidleukemia in patients who are ineligible for intensivechemotherapy. Ther Adv Hematol 10:204062071988282. https://doi.org/10.1177/2040620719882822
doi: 10.1177/2040620719882822
Lam SSY, Leung AYH (2020) Overcoming resistance to FLT3 inhibitors in the treatment of FLT3-mutated AML. Int J Mol Sci. https://doi.org/10.3390/IJMS21041537
doi: 10.3390/IJMS21041537
pubmed: 33317061
pmcid: 7764374
Konopleva MY (2021) Mechanisms for resistance in AML insights into molecular pathways mediating resistance to venetoclax. Best Pract Res Clin Haematol. https://doi.org/10.1016/J.BEHA.2021.101251
doi: 10.1016/J.BEHA.2021.101251
pubmed: 33762105
Xie Y, Yuan X, Zhou W et al (2020) The circular RNA HIPK3 (circHIPK3) and its regulation in cancer progression: review. Life Sci 254:117252. https://doi.org/10.1016/J.LFS.2019.117252
doi: 10.1016/J.LFS.2019.117252
pubmed: 31901445
Liang J, Shen YC, Zhang XY et al (2020) Circular RNA HIPK3 downregulation mediates hydrogen peroxide-induced cytotoxicity in human osteoblasts. Aging (Albany NY) 12:1159–1170. https://doi.org/10.18632/AGING.102674
doi: 10.18632/AGING.102674
pubmed: 31955154